Abstract:The expression of sarcoplasmic reticulum SERCA1a Ca 2+ -ATPase wild-type and D351E mutants was optimized in yeast under the control of a galactose promoter. Fully active wild-type enzyme was recovered in yeast microsomal membrane fractions in sufficient amounts to permit a rapid and practical assay of ATP hydrolysis and phosphoenzyme formation from ATP or Pi. Mutant and wild-type Ca 2+ -ATPase were assayed for phosphorylation by Pi under conditions that are known to facilitate this reaction in the wild-type en… Show more
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